Disease relevance of Mmp1

• In the proximity of the colon stenosis, total matrix metalloproteinase activity and matrix metalloproteinase-2 were significantly (P < 0.05) higher above than below the obstruction [1].
• Suppression of prostate cancer invasive potential and matrix metalloproteinase activity by E-cadherin transfection [2].
• METHODS: We used a rat model of myocardial infarction (MI) complicated by various degrees of left ventricular dysfunction and atrial dilation to study fibrosis and matrix metalloproteinase (MMP) activity in the left atrial (LA) myocardium by means of histologic, Western blot, zymographic, and immunohistologic techniques [3].
• Matrix metalloproteinase expression increases after cerebral focal ischemia in rats: inhibition of matrix metalloproteinase-9 reduces infarct size [4].
• Influence of therapeutic hypothermia on matrix metalloproteinase activity after traumatic brain injury in rats [5].

Psychiatry related information on Mmp1

• The periovulatory increase in ovarian matrix metalloproteinase inhibitor (MMPI) expression is regulated both in vitro and in vivo by LH, but the intermediary steps in this process are uncertain [6].

High impact information on Mmp1

• Elastase and matrix metalloproteinase inhibitors induce regression, and tenascin-C antisense prevents progression, of vascular disease [7].
• Western blot and immunohistochemical analyses confirmed that interstitial collagenase protein appears in association with the loss of amnion type I collagen [8].
• Livers were analyzed for evidence of matrix degradation, matrix metalloproteinase (MMP) and tissue inhibitor of metalloproteinase (TIMP) expression, stellate cell apoptosis, tissue transglutaminase (tTg) expression, and matrix cross-linking during spontaneous recovery of up to 366 days [9].
• Because this enzyme degrades a wide spectrum of normal basement membrane proteins and activates progelatinase B and interstitial collagenase, it may have an important role in liver injury and fibrosis [10].
• Stimulation of interstitial collagenase in co-cultures of rat hepatocytes and sinusoidal cells [11].

Chemical compound and disease context of Mmp1

• After 1 month of treatment, the left ventricular weight/body weight ratio (LVW/BW), changes in myosin heavy chain expression (MHC), matrix metalloproteinase (MMP)-2 activity, the collagen I/III ratio, and the expression of ERs and Ang II receptors in the LV were evaluated [12].
• Furthermore, ramipril reduced fibrosis by enhanced interstitial collagenase expression [13].
• STUDY OBJECTIVES: To evaluate the effects of L-arginine on acute pulmonary embolism (APE)-induced pulmonary hypertension and increases in lung matrix metalloproteinase (MMP)-2 and MMP-9 activities [14].
• In the current study, doxycycline and 5 different CMTs were tested to prevent matrix metalloproteinase (MMP)-dependent periodontal tissue breakdown in an animal model of periodontitis [15].
• Preventive versus treatment effect of AG3340, a potent matrix metalloproteinase inhibitor in a rat model of choroidal neovascularization [16].

Biological context of Mmp1

• Divergent patterns of matrix metalloproteinase activity during wound healing in ileum and colon of rats [17].
• Stress-deprivation for 24 hr resulted in a marked upregulation in MMP-1 expression [18].
• We screened cDNA libraries and we found that six matrix metalloproteinase genes were highly expressed during rat skin wound healing [19].
• TGF-beta plays a key role in morphogenesis of the pancreatic islets of Langerhans by controlling the activity of the matrix metalloproteinase MMP-2 [20].
• Inhibition of matrix metalloproteinase activity inhibits smooth muscle cell migration but not neointimal thickening after arterial injury [21].

Anatomical context of Mmp1

• The wound fluid and the neosynthetized connective tissue deposited in the chambers were collected and analyzed for matrix metalloproteinase expression and/or activity [22].
• The results of our study demonstrate that MMP-1 expression in tendon cells can be modulated by varying amplitudes and frequencies of cyclic tensile strain, presumably through a cytoskeletally based mechanotransduction pathway [18].
• To understand better the nature of this neutral proteinase in the rat myocardium, myocardial collagenase was purified to homogeneity [23].
• Disruption of the actin cytoskeleton with cytochalasin D abolished all inhibitory effects of cyclic strain on MMP-1 expression [18].
• Expression of matrix metalloproteinase genes in transformed rat cell lines of high and low metastatic potential [24].

Associations of Mmp1 with chemical compounds

• Rapid release of matrix metalloproteinase (MMP)-2 by thrombin in the rat aorta: modulation by protein tyrosine kinase/phosphatase [25].
• Increased angiotensin II (Ang II), matrix metalloproteinase type II (MMP2), and sympathetic activity accompany age-associated arterial remodeling [26].
• Angiotensin II activates matrix metalloproteinase type II and mimics age-associated carotid arterial remodeling in young rats [26].
• Dexamethasone regulation of matrix metalloproteinase expression in CNS vascular endothelium [27].
• Ventilator-induced lung injury upregulates and activates gelatinases and EMMPRIN: attenuation by the synthetic matrix metalloproteinase inhibitor, Prinomastat (AG3340) [28].

Physical interactions of Mmp1

• In the present study we investigated whether matrix metalloproteinase (MMP) binding to elastin and elastin degradation is prevented by AlCl(3) pretreatment [29].

Regulatory relationships of Mmp1

• Gonadotropin-releasing hormone agonist has the ability to induce increased matrix metalloproteinase (MMP)-2 and membrane type 1-MMP expression in corpora lutea, and structural luteolysis in rats [30].
• We previously reported that prolactin (PRL) stimulated matrix metalloproteinase (MMP)-2 activity to degrade collagen type IV as a mechanism of structural luteolysis [30].
• Treatment of rats with the LOX-1 antibody prevented I/R-induced upregulation of LOX-1 and reduced MMP-1 and adhesion molecule expression as well as leukocyte recruitment [31].
• We recently demonstrated that IGFs inhibit bone collagen degradation, and we postulated that they may either inhibit the expression of interstitial collagenase or stimulate the synthesis of tissue inhibitors of metalloproteinase-1 (TIMP-1), -2, or -3 [32].
• Basic fibroblast growth factor stimulates expression of interstitial collagenase and inhibitors of metalloproteinases in rat bone cells [33].

Other interactions of Mmp1

• These studies indicate that a discrete matrix metalloproteinase, gelatinase A, is capable of inducing the complex genetic rearrangements that characterize renal tubular epithelial-mesenchymal transformation [34].
• HAL (200 nm) up-regulated matrix metalloproteinase (MMP)-3 and MMP-13 expression between 10- and 50-fold, resulting in a 2- to 3-fold increase of interstitial collagenase activity [35].
• This decline in glomerular gelatinolytic activity was due to a reduction in gelatinase B [matrix metalloproteinase (MMP)-9] [36].
• Gene expression of matrix metalloproteinase ( MMP) and tissue inhibitor of metalloproteinase ( TIMP) was measured by RT-PCR and type IV collagen content by immunohistochemistry [37].
• Matrix metalloproteinase induction by EMMPRIN in experimental focal cerebral ischemia [38].

Analytical, diagnostic and therapeutic context of Mmp1

• A single band of purified interstitial collagenase was observed on Western blot analysis [23].
• The present study utilized reverse transcriptase-polymerase chain reaction (RT-PCR) to explore the expression of MMP-1 and MMP-2 genes in the PFS and SS in P8 and P32 rats, and also to determine whether these MMP genes are modulated by exogenous mechanical forces [39].
• Consistent with past findings [19], lung injury was accompanied by an accumulation of matrix metalloproteinase 9 (MMP-9) in bronchoalveolar lavage (BAL) fluid [40].
• The allograft microenvironment was examined using immunohistochemistry for fibrogenic markers (transforming growth factor [TGF]-beta, platelet-derived growth factor [PDGF], tissue plasminogen activator [TPA], plasminogen activator inhibitor [PAI]-1, matrix metalloproteinase [MMP]-2, and tissue inhibitor of matrix metalloproteinase [TIMP]-2) [41].
• Collagenase activity, measured by zymography, and expression of matrix metalloproteinase (MMP-1) and tissue inhibitor of metalloproteinase (TIMP) mRNA, detected by Northern blotting and in situ hybridization, in the rat heart 6 h to 28 days after left coronary artery ligation were studied [42].

References